scholarly journals Inside Cover: Synthesis and Structural Characterization of Homochiral Homo-oligomers of Parent cis- and trans-Furanoid-β-Amino Acids (Chem. Eur. J. 46/2011)

2011 ◽  
Vol 17 (46) ◽  
pp. 12834-12834
Author(s):  
Sunil K. Pandey ◽  
Ganesh F. Jogdand ◽  
João C. A. Oliveira ◽  
Ricardo A. Mata ◽  
Pattuparambil R. Rajamohanan ◽  
...  
2012 ◽  
Vol 2012 (13) ◽  
pp. 2656-2663 ◽  
Author(s):  
Awadut G. Giri ◽  
Ganesh F. Jogdand ◽  
Pattuparampil R. Rajamohanan ◽  
Sunil K. Pandey ◽  
Chepuri V. Ramana

2011 ◽  
Vol 17 (46) ◽  
pp. 12946-12954 ◽  
Author(s):  
Sunil K. Pandey ◽  
Ganesh F. Jogdand ◽  
João C. A. Oliveira ◽  
Ricardo A. Mata ◽  
Pattuparambil R. Rajamohanan ◽  
...  

2015 ◽  
Vol 39 (5) ◽  
pp. 3319-3326 ◽  
Author(s):  
Madhusudana M. B. Reddy ◽  
K. Basuroy ◽  
S. Chandrappa ◽  
B. Dinesh ◽  
B. Vasantha ◽  
...  

γn amino acid residues can be incorporated into structures in γn and hybrid sequences containing folded and extended α and δ residues.


Author(s):  
Jolanta Cieślak ◽  
Akimasa Miyanaga ◽  
Makoto Takaishi ◽  
Fumitaka Kudo ◽  
Tadashi Eguchi

Adenylation enzymes play an important role in the selective incorporation of the cognate carboxylate substrates in natural product biosynthesis. Here, the biochemical and structural characterization of the adenylation enzyme IdnL7, which is involved in the biosynthesis of the macrolactam polyketide antibiotic incednine, is reported. Biochemical analysis showed that IdnL7 selects and activates several small amino acids. The structure of IdnL7 in complex with an L-alanyl-adenylate intermediate mimic, 5′-O-[N-(L-alanyl)sulfamoyl]adenosine, was determined at 2.1 Å resolution. The structure of IdnL7 explains the broad substrate specificity of IdnL7 towards small L-amino acids.


Author(s):  
Michela Cattabriga ◽  
Andrea Marchi ◽  
Lorenza Marvelli ◽  
Roberto Rossi ◽  
Gianni Vertuani ◽  
...  

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